Nucleic Acids Research, 1983, Vol. 11, No. 21 7435-7452
© 1983
MOLECULAR BIOLOGY |
The bacteriopbage 
O replication protein: isolation and characterization of the amplified initiator
Department of Biochemistry, School of Hygiene and Public Health, The Johns Hopkins University 615 North Wolfe Street, Baltimore, MD 21205, USA
Received July 11, 1983. Revised September 26, 1983. Accepted September 26, 1983.
The bacteriophage 
0 protein participates in the Initiation of DMA replication. The Q. gene was cloned into plasmid pKC30 ouch that its expression was controlled by the PL promoter. A prophage-coded thennosensitlve cI repressor was used to regulate transcription of the cloned Q. gene. Thermal inactivation of the cI repressor resulted in overproduction of the O protein until it constituted approximately 20% of the total cellular protein of Each-arlohla coll. A simple three-step purification protocol was developed that yields several milligrams of homogeneous O protein per gram of cell paste. The precise position of the Q. gene in the known DNA sequence was identified from the amino-terminal sequence of the isolated O protein. Purified O protein stimulated the replication of plasmid dv DNA in vitro and specifically bound to duplex DNA fragments carrying the replication origin.
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